4K02
Crystal structure of AtDHNAT1, a 1,4-dihydroxy-2-naphthoyl-CoA thioesterase from Arabidopsis thaliana
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 110 |
| Detector technology | CCD |
| Collection date | 2012-03-21 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.033 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 99.529, 99.529, 61.257 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 28.880 - 1.900 |
| R-factor | 0.18451 |
| Rwork | 0.183 |
| R-free | 0.21055 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1sc0 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.618 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 28.880 | 1.950 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.058 | 0.764 |
| Number of reflections | 26984 | |
| <I/σ(I)> | 48.8 | 2.4 |
| Completeness [%] | 96.4 | 84.1 |
| Redundancy | 35.3 | 22.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 298 | 2.7 M NaHCOOH, 100 mM Tris-HCl, 10 mM n-octyl- D-glucoside in protein, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
